ITA3_HUMAN
ID ITA3_HUMAN Reviewed; 1051 AA.
AC P26006; A7E246; B7ZM80; B9EGQ1; D3DTX4; D3DTX5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 5.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Integrin alpha-3;
DE AltName: Full=CD49 antigen-like family member C;
DE AltName: Full=FRP-2;
DE AltName: Full=Galactoprotein B3;
DE Short=GAPB3;
DE AltName: Full=VLA-3 subunit alpha;
DE AltName: CD_antigen=CD49c;
DE Contains:
DE RecName: Full=Integrin alpha-3 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-3 light chain;
DE Flags: Precursor;
GN Name=ITGA3; Synonyms=MSK18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=1655803; DOI=10.1083/jcb.115.1.257;
RA Takada Y., Murphy E., Pil P., Chen C., Ginsberg M.H., Hemler M.E.;
RT "Molecular cloning and expression of the cDNA for alpha 3 subunit of human
RT alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, laminin, and
RT collagen.";
RL J. Cell Biol. 115:257-266(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-1051 (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=1714443; DOI=10.1093/oxfordjournals.jbchem.a123436;
RA Tsuji T., Hakomori S., Osawa T.;
RT "Identification of human galactoprotein b3, an oncogenic transformation-
RT induced membrane glycoprotein, as VLA-3 alpha subunit: the primary
RT structure of human integrin alpha 3.";
RL J. Biochem. 109:659-665(1991).
RN [7]
RP PROTEIN SEQUENCE OF 33-49.
RX PubMed=8187758; DOI=10.1002/j.1460-2075.1994.tb06479.x;
RA Ohta H., Tsurudome M., Matsumura H., Koga Y., Morikawa S., Kawano M.,
RA Kusugawa S., Komada H., Nishio M., Ito Y.;
RT "Molecular and biological characterization of fusion regulatory proteins
RT (FRPs): anti-FRP mAbs induced HIV-mediated cell fusion via an integrin
RT system.";
RL EMBO J. 13:2044-2055(1994).
RN [8]
RP PROTEIN SEQUENCE OF 33-46.
RX PubMed=3033641; DOI=10.1073/pnas.84.10.3239;
RA Takada Y., Strominger J.L., Hemler M.E.;
RT "The very late antigen family of heterodimers is part of a superfamily of
RT molecules involved in adhesion and embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987).
RN [9]
RP PROTEIN SEQUENCE OF 33-40, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH FAP.
RX PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
RA Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
RA Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
RT "A novel protease-docking function of integrin at invadopodia.";
RL J. Biol. Chem. 274:24947-24952(1999).
RN [10]
RP ALTERNATIVE SPLICING, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=9111516;
RA de Melker A.A., Sterk L.M., Delwel G.O., Fles D.L., Daams H., Weening J.J.,
RA Sonnenberg A.;
RT "The A and B variants of the alpha 3 integrin subunit: tissue distribution
RT and functional characterization.";
RL Lab. Invest. 76:547-563(1997).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=14596610; DOI=10.1021/bi034726u;
RA Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.;
RT "Mass spectrometric based mapping of the disulfide bonding patterns of
RT integrin alpha chains.";
RL Biochemistry 42:12950-12959(2003).
RN [12]
RP PALMITOYLATION AT CYS-1016, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-1016.
RX PubMed=15611341; DOI=10.1083/jcb.200404100;
RA Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
RT "Palmitoylation supports assembly and function of integrin-tetraspanin
RT complexes.";
RL J. Cell Biol. 167:1231-1240(2004).
RN [13]
RP INTERACTION WITH ITGB1; LGALS3 AND CSPG4, AND FUNCTION.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=32487760; DOI=10.1128/mbio.01087-20;
RA Alqarihi A., Gebremariam T., Gu Y., Swidergall M., Alkhazraji S.,
RA Soliman S.S.M., Bruno V.M., Edwards J.E. Jr., Filler S.G., Uppuluri P.,
RA Ibrahim A.S.;
RT "GRP78 and Integrins Play Different Roles in Host Cell Invasion during
RT Mucormycosis.";
RL MBio 11:e01087-e01087(2020).
RN [16]
RP VARIANT ILNEB PRO-628.
RX PubMed=22512483; DOI=10.1056/nejmoa1110813;
RA Has C., Sparta G., Kiritsi D., Weibel L., Moeller A., Vega-Warner V.,
RA Waters A., He Y., Anikster Y., Esser P., Straub B.K., Hausser I.,
RA Bockenhauer D., Dekel B., Hildebrandt F., Bruckner-Tuderman L., Laube G.F.;
RT "Integrin alpha3 mutations with kidney, lung, and skin disease.";
RL N. Engl. J. Med. 366:1508-1514(2012).
RN [17]
RP VARIANTS ILNEB ARG-125 AND GLN-274.
RX PubMed=27717396; DOI=10.1186/s13023-016-0514-z;
RA Colombo E.A., Spaccini L., Volpi L., Negri G., Cittaro D., Lazarevic D.,
RA Zirpoli S., Farolfi A., Gervasini C., Cubellis M.V., Larizza L.;
RT "Viable phenotype of ILNEB syndrome without nephrotic impairment in
RT siblings heterozygous for unreported integrin alpha3 mutations.";
RL Orphanet J. Rare Dis. 11:136-136(2016).
CC -!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin,
CC laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC 3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC plasma membranes in a collagen-dependent manner and hence may
CC participate in the adhesion, formation of invadopodia and matrix
CC degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC migration. {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:15181153}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA3:ITGB1 may act as a
CC receptor for R.delemar CotH7 in alveolar epithelial cells, which may be
CC an early step in pulmonary mucormycosis disease progression.
CC {ECO:0000269|PubMed:32487760}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-3 associates with beta-1. Interacts with HPS5. Interacts with FAP
CC (seprase); the interaction occurs at the cell surface of invadopodia
CC membrane in a collagen-dependent manner. {ECO:0000269|PubMed:10455171,
CC ECO:0000269|PubMed:15181153}.
CC -!- INTERACTION:
CC P26006; P48509: CD151; NbExp=6; IntAct=EBI-2550768, EBI-10210332;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15611341,
CC ECO:0000269|PubMed:32487760}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15611341}; Lipid-
CC anchor {ECO:0000269|PubMed:15611341}. Cell projection, invadopodium
CC membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane
CC protein {ECO:0000255}. Cell projection, filopodium membrane
CC {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Enriched preferentially at invadopodia, cell
CC membrane protrusions that correspond to sites of cell invasion, in a
CC collagen-dependent manner. {ECO:0000269|PubMed:10455171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha-3A;
CC IsoId=P26006-2; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-3B;
CC IsoId=P26006-1; Sequence=VSP_002721;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is
CC expressed in brain and heart. In brain, both isoforms are exclusively
CC expressed on vascular smooth muscle cells, whereas in heart isoform 1
CC is strongly expressed on vascular smooth muscle cells, isoform 2 is
CC detected only on endothelial vein cells. {ECO:0000269|PubMed:9111516}.
CC -!- PTM: Isoform 1, but not isoform 2, is phosphorylated on serine
CC residues. Phosphorylation increases after phorbol 12-myristate 13-
CC acetate stimulation. {ECO:0000269|PubMed:9111516}.
CC -!- DISEASE: Interstitial lung disease, nephrotic syndrome, and
CC epidermolysis bullosa, congenital (ILNEB) [MIM:614748]: A multiorgan
CC disorder characterized by congenital nephrotic syndrome, interstitial
CC lung disease, and epidermolysis bullosa. The respiratory and renal
CC features predominate, and lung involvement accounts for the lethal
CC course of the disease. {ECO:0000269|PubMed:22512483,
CC ECO:0000269|PubMed:27717396}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- BIOTECHNOLOGY: Antibodies against integrin alpha-3 ITGA3 protects
CC epithelial cells from invasion by the fungus R.delemar, a causative
CC agent of mucormycosis, and could thus potentially be used to treat
CC mucormycosis disease. {ECO:0000305|PubMed:32487760}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; M59911; AAA36120.1; -; mRNA.
DR EMBL; AK289961; BAF82650.1; -; mRNA.
DR EMBL; AC002401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94645.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94646.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94647.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94648.1; -; Genomic_DNA.
DR EMBL; BC136636; AAI36637.1; -; mRNA.
DR EMBL; BC144328; AAI44329.1; -; mRNA.
DR EMBL; BC150190; AAI50191.1; -; mRNA.
DR EMBL; D01038; BAA00845.1; -; mRNA.
DR CCDS; CCDS11558.1; -. [P26006-2]
DR PIR; A40021; A40021.
DR RefSeq; NP_002195.1; NM_002204.3. [P26006-2]
DR AlphaFoldDB; P26006; -.
DR SMR; P26006; -.
DR BioGRID; 109882; 74.
DR ComplexPortal; CPX-1797; Integrin alpha3-beta1 complex.
DR CORUM; P26006; -.
DR DIP; DIP-140N; -.
DR IntAct; P26006; 29.
DR MINT; P26006; -.
DR STRING; 9606.ENSP00000007722; -.
DR BindingDB; P26006; -.
DR ChEMBL; CHEMBL3525; -.
DR GuidetoPHARMACOLOGY; 2442; -.
DR GlyConnect; 738; 3 N-Linked glycans (2 sites).
DR GlyGen; P26006; 15 sites, 5 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P26006; -.
DR PhosphoSitePlus; P26006; -.
DR SwissPalm; P26006; -.
DR BioMuta; ITGA3; -.
DR DMDM; 347595830; -.
DR EPD; P26006; -.
DR jPOST; P26006; -.
DR MassIVE; P26006; -.
DR MaxQB; P26006; -.
DR PaxDb; P26006; -.
DR PeptideAtlas; P26006; -.
DR PRIDE; P26006; -.
DR ProteomicsDB; 54305; -. [P26006-2]
DR ProteomicsDB; 54306; -. [P26006-1]
DR ABCD; P26006; 39 sequenced antibodies.
DR Antibodypedia; 18000; 1064 antibodies from 42 providers.
DR DNASU; 3675; -.
DR Ensembl; ENST00000007722.11; ENSP00000007722.7; ENSG00000005884.18. [P26006-1]
DR Ensembl; ENST00000320031.13; ENSP00000315190.8; ENSG00000005884.18. [P26006-2]
DR GeneID; 3675; -.
DR KEGG; hsa:3675; -.
DR MANE-Select; ENST00000320031.13; ENSP00000315190.8; NM_002204.4; NP_002195.1.
DR UCSC; uc010dbl.4; human. [P26006-2]
DR CTD; 3675; -.
DR DisGeNET; 3675; -.
DR GeneCards; ITGA3; -.
DR HGNC; HGNC:6139; ITGA3.
DR HPA; ENSG00000005884; Low tissue specificity.
DR MalaCards; ITGA3; -.
DR MIM; 605025; gene.
DR MIM; 614748; phenotype.
DR neXtProt; NX_P26006; -.
DR OpenTargets; ENSG00000005884; -.
DR Orphanet; 306504; Interstitial lung disease-nephrotic syndrome-epidermolysis bullosa syndrome.
DR PharmGKB; PA29939; -.
DR VEuPathDB; HostDB:ENSG00000005884; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157746; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; P26006; -.
DR OMA; RYNHTGA; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P26006; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR SignaLink; P26006; -.
DR SIGNOR; P26006; -.
DR BioGRID-ORCS; 3675; 37 hits in 1076 CRISPR screens.
DR ChiTaRS; ITGA3; human.
DR GeneWiki; CD49c; -.
DR GenomeRNAi; 3675; -.
DR Pharos; P26006; Tchem.
DR PRO; PR:P26006; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P26006; protein.
DR Bgee; ENSG00000005884; Expressed in metanephric glomerulus and 108 other tissues.
DR ExpressionAtlas; P26006; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; ISS:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISS:ARUK-UCL.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0097062; P:dendritic spine maintenance; ISS:ARUK-UCL.
DR GO; GO:0035640; P:exploration behavior; ISS:ARUK-UCL.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0031345; P:negative regulation of cell projection organization; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:ARUK-UCL.
DR GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0097205; P:renal filtration; IMP:UniProtKB.
DR GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disease variant; Disulfide bond;
KW Epidermolysis bullosa; Glycoprotein; Integrin; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:10455171,
FT ECO:0000269|PubMed:3033641, ECO:0000269|PubMed:8187758"
FT CHAIN 33..1051
FT /note="Integrin alpha-3"
FT /id="PRO_0000016238"
FT CHAIN 33..872
FT /note="Integrin alpha-3 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016239"
FT CHAIN 876..1051
FT /note="Integrin alpha-3 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016240"
FT TOPO_DOM 33..991
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1051
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..103
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 110..171
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 185..235
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 236..292
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 293..354
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 356..411
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 415..477
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 855..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1021
FT /note="Interaction with HPS5"
FT MOTIF 1017..1021
FT /note="GFFKR motif"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT LIPID 1016
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15611341"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 140..162
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 185..197
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 485..490
FT /evidence="ECO:0000250"
FT DISULFID 496..550
FT /evidence="ECO:0000250"
FT DISULFID 615..621
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 694..702
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 846..904
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 911..916
FT /evidence="ECO:0000269|PubMed:14596610"
FT VAR_SEQ 1017..1051
FT /note="GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DFFKRTRYYQIMP
FT KYHAVRIREEERYPPPGSTLPTKKHWVTSWQTRDQYY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1655803"
FT /id="VSP_002721"
FT VARIANT 125
FT /note="G -> R (in ILNEB)"
FT /evidence="ECO:0000269|PubMed:27717396"
FT /id="VAR_077512"
FT VARIANT 268
FT /note="I -> F (in dbSNP:rs2230390)"
FT /id="VAR_055967"
FT VARIANT 274
FT /note="R -> Q (in ILNEB; dbSNP:rs745505565)"
FT /evidence="ECO:0000269|PubMed:27717396"
FT /id="VAR_077513"
FT VARIANT 628
FT /note="R -> P (in ILNEB; dbSNP:rs140781106)"
FT /evidence="ECO:0000269|PubMed:22512483"
FT /id="VAR_068808"
FT VARIANT 719
FT /note="A -> T (in dbSNP:rs2230392)"
FT /id="VAR_055968"
FT VARIANT 840
FT /note="G -> S (in dbSNP:rs2301626)"
FT /id="VAR_055969"
FT MUTAGEN 1016
FT /note="C->S: Abolishes palmitoylation."
FT /evidence="ECO:0000269|PubMed:15611341"
SQ SEQUENCE 1051 AA; 116612 MW; EEAFA7778EF17B21 CRC64;
MGPGPSRAPR APRLMLCALA LMVAAGGCVV SAFNLDTRFL VVKEAGNPGS LFGYSVALHR
QTERQQRYLL LAGAPRELAV PDGYTNRTGA VYLCPLTAHK DDCERMNITV KNDPGHHIIE
DMWLGVTVAS QGPAGRVLVC AHRYTQVLWS GSEDQRRMVG KCYVRGNDLE LDSSDDWQTY
HNEMCNSNTD YLETGMCQLG TSGGFTQNTV YFGAPGAYNW KGNSYMIQRK EWDLSEYSYK
DPEDQGNLYI GYTMQVGSFI LHPKNITIVT GAPRHRHMGA VFLLSQEAGG DLRRRQVLEG
SQVGAYFGSA IALADLNNDG WQDLLVGAPY YFERKEEVGG AIYVFMNQAG TSFPAHPSLL
LHGPSGSAFG LSVASIGDIN QDGFQDIAVG APFEGLGKVY IYHSSSKGLL RQPQQVIHGE
KLGLPGLATF GYSLSGQMDV DENFYPDLLV GSLSDHIVLL RARPVINIVH KTLVPRPAVL
DPALCTATSC VQVELCFAYN QSAGNPNYRR NITLAYTLEA DRDRRPPRLR FAGSESAVFH
GFFSMPEMRC QKLELLLMDN LRDKLRPIII SMNYSLPLRM PDRPRLGLRS LDAYPILNQA
QALENHTEVQ FQKECGPDNK CESNLQMRAA FVSEQQQKLS RLQYSRDVRK LLLSINVTNT
RTSERSGEDA HEALLTLVVP PALLLSSVRP PGACQANETI FCELGNPFKR NQRMELLIAF
EVIGVTLHTR DLQVQLQLST SSHQDNLWPM ILTLLVDYTL QTSLSMVNHR LQSFFGGTVM
GESGMKTVED VGSPLKYEFQ VGPMGEGLVG LGTLVLGLEW PYEVSNGKWL LYPTEITVHG
NGSWPCRPPG DLINPLNLTL SDPGDRPSSP QRRRRQLDPG GGQGPPPVTL AAAKKAKSET
VLTCATGRAH CVWLECPIPD APVVTNVTVK ARVWNSTFIE DYRDFDRVRV NGWATLFLRT
SIPTINMENK TTWFSVDIDS ELVEELPAEI ELWLVLVAVG AGLLLLGLII LLLWKCGFFK
RARTRALYEA KRQKAEMKSQ PSETERLTDD Y
